Language：English   Publishing type：Research paper (scientific journal)  

DOI： https://doi.org/10.3389/fmicb.2020.00885

Other Link： https://www.frontiersin.org/articles/10.3389/fmicb.2020.00885/full

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1186/s12934-020-01385-2

Other Link： https://microbialcellfactories.biomedcentral.com/articles/10.1186/s12934-020-01385-2

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1128/genomeA.01596-16

Other Link： http://genomea.asm.org/content/5/5/e01596-16

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1007/s10529-016-2118-z

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1128/genomeA.00360-16

Language：English   Publishing type：Research paper (scientific journal)  

Language：English   Publishing type：Research paper (scientific journal)  

A filamentous bacteriophage, φOH3, was isolated from hot spring sediment in Obama hot spring in Japan with the hyperthermophilic bacterium Thermus thermophilus HB8 as its host. Phage φOH3, which was classified into the Inoviridae family, consists of a flexible filamentous particle 830 nm long and 8 nm wide. φOH3 was stable at temperatures ranging from 70 to 90°C and at pHs ranging from 6 to 9. A one-step growth curve of the phage showed a 60-min latent period beginning immediately postinfection, followed by intracellular virus particle production during the subsequent 40 min. The released virion number of φOH3 was 109. During the latent period, both single stranded DNA (ssDNA) and the replicative form (RF) of phage DNA were multiplied from min 40 onward. During the release period, the copy numbers of both ssDNA and RF DNA increased sharply. The size of the φOH3 genome is 5688 bp, and eight putative open reading frames (ORFs) were annotated. These ORFs were encoded on the plus strand of RF DNA and showed no significant homology with any known phage genes, except ORF 5, which showed 60% identity with the gene VIII product of the Thermus filamentous phage PH75. All the ORFs were similar to predicted genes annotated in the Thermus aquaticus Y51MC23 and Meiothermus timidus DSM 17022 genomes at the amino acid sequence level. This is the first report of the whole genome structure and DNA multiplication of a filamentous T. thermophilus phage within its host cell.

Language：English   Publishing type：Research paper (scientific journal)  

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Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1007/s10529-014-1597-z

Language：English   Publishing type：Research paper (scientific journal)  

DOI： http://dx.doi.org/10.1016/j.enzmictec.2014.04.002

Language：English   Publishing type：Research paper (scientific journal)  

DOI： http://dx.doi.org/10.1155/2014/195305

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1186/2193-1801-2-691

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1128/JB.00709-13

Language：English   Publishing type：Research paper (scientific journal)  

DOI： http://dx.doi.org/10.1271/bbb.130492

Language：English   Publishing type：Research paper (scientific journal)  

DOI： http://dx.doi.org/10.1016/j.molcatb.2013.04.013

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1186/2193-1801-2-485

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.4236/aim.2013.33038

Language：English   Publishing type：Research paper (scientific journal)  

Other Link： http://link.springer.com/article/10.1007%2Fs00792-013-0527-7

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1007/s00253-013-4902-1

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1128/genomeA.00156-12

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1128/genomeA.00156-12

Language：English   Publishing type：Research paper (scientific journal)  

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TA thermostable, NADP?-dependent D- amino acid dehydrogenase (DAADH) was created from the meso-diaminopimelate dehydrogenase of Ureibacillus thermosphaericus strain A1 by introducing five point mutations into amino acid residues located in the active site. The recombinant protein, expressed in Escherichia coli, was purified to homogeneity using a two-step separation procedure and then characterized. In the presence of NADP?, the protein catalyzed the oxidative deamination of several D-amino acids, including D-cyclohexylalanine, D-isoleucine and D-2-aminooctanoate, but not meso- diaminopimelate, confirming the creation of a NADP-dependent DAADH. For the reverse reaction, the corresponding 2-oxo acids were aminated in the presence of NADPH and ammonia. In addition, the D-amino acid dehydrogenase showed no loss of activity at 65 °C, indicating the mutant enzyme was more thermostable than its parental meso-diaminopimelate dehydrogenase.

DOI： 10.1007/s10529-012-0952-1

Language：English   Publishing type：Research paper (scientific journal)  

The sporulation inhibitory gene spi in the pock-forming conjugative plasmid pSA1.1 of Streptomyces azureus was introduced into cells via a high or low copy number vector to examine the effect of gene dosage on the growth of Streptomyces lividans TK24 as a host. In transformants carrying a high spi copy number, nutrient mycelial growth was inhibited, as was morphological differentiation from substrate mycelium to aerial mycelium on solid media. The degree of inhibition depended on the spi gene dosage, but the presence of pSA1.1 imp genes, which encode negative repressor proteins for spi, relieved the inhibition. Confocal images of Spi tagged with enhanced green fluorescent protein in cells on solid media revealed that spi expression was initiated at the time of elongation of substrate mycelium, that its expression increased dramatically at septation in aerial hyphae, and that the expression was maximal during prespore formation. Expression of spi covered the whole of the hyphae, and the level of expression at the tip of the hyphae during prespore formation was about sixfold greater than during substrate mycelial growth and threefold greater than during aerial mycelial growth. Thus, localized expression of spi at particular times may inhibit sporulation until triggering imp expression to repress its inhibitory effects.

DOI： 10.1007/s00253-012-4000-9

Language：English   Publishing type：Research paper (scientific journal)  

To elucidate the mechanism of silica biodeposition in hot spring water, which is induced by Al(3+) ions bound to the surface of microbes, a chelate resin (Chelex 100) was used as a model compound of the surface of microbes. No silicic acid was adsorbed on the Na type Chelex 100, whereas silicic acids were significantly adsorbed to the Al type Chelex 100. In the Al type Chelex 100, the Al(3+) ions were present as 1:1 tridentate complex with iminodiacetate (IDA) group. After adsorption of silicic acid to Al type Chelex 100, a IDAAlOSi(OH)(3) site formed. The site acted as a template for the successive adsorption of silicic acids to form silica sheets around Al type Chelex 100 particles. In conclusion, Al(3+) ions bound to the surface of microbes play a key role as a trigger for the biodeposition of silica in hot spring water.

DOI： 10.1016/j.colsurfb.2012.02.044

Language：English   Publishing type：Research paper (scientific journal)  

Application of microorganisms as surface modifiers in flocculation has generated a great deal of interest in recent times. The surface properties such as zeta-potential and hydrophobicity of minerals and microorganisms play a major role in determining the adsorption of microorganisms onto the minerals and hence the efficiency of flocculation. The utility of microorganisms, including Escherichia coli (wild-type and genetically modified strain Sip), Arthrobacter nicotianae, Bacillus licheniformis, and Pseudomonas maltophilia, has been evaluated by measuring their zeta-potentials and carrying out adsorption and flocculation experiments. Of the tested microorganisms, adsorption of E. coli strain Sip significantly modified the quartz surface. The zeta-potential of the quartz became highly positive at acidic pH, and its IEP (isoelectric point) was shifted from pH < 2 to pH 4.3. Moreover, the settling velocity of the bio-treated quartz reached its maximum value at this pH. The number of cells adsorbed onto quartz was low at pH above the IEP due to the identical surface charges of the mineral and bacterial cells. This led to a repulsive force between the mineral particles and bacterial cells, which hindered the adsorption process. For all of the studied strains, the settling velocity of bio-treated quartz was high at their respective IEPs. An interaction model of microorganisms is proposed to explain the flocculation behavior of bio-treated quartz. Potential energies were calculated using the DLVO theory, and the results were found to be in good agreement with the flocculation tests. The settling velocity of the bio-treated quartz was maximized at pH close to the IEP of microbial cells. Interaction between cells is identified as the most likely cause of flocculation of bio-treated quartz.

DOI： 10.1016/j.minpro.2011.10.001

Language：English   Publishing type：Research paper (scientific journal)  

We screened various thermophiles for meso-diaminopimelate dehydrogenase (meso-DAPDH, EC 1.4.1.16), which catalyzes the NAD(P)-dependent oxidative deamination of meso-diaminopimelate, and found the enzyme in a thermophilic bacterium isolated from compost in Japan. The bacterium grew well aerobically at around 55°C and was identified as Ureibacillus thermosphaericus strain A1. We purified the enzyme about 47-fold to homogeneity from crude cell extract using five successive purification steps. The molecular mass of the purified protein was about 80 kDa, and the molecule consists of a homodimer with the subunit molecular mass of about 40 kDa. The optimum pH and temperature for the catalytic activity of the enzyme are about 10.5 and 65°C, respectively. The enzyme is highly selective for meso-diaminopimelate as the electron donor, and NADP but not NAD can serve as the electron acceptor. The Km values for meso-diaminopimelate and NADP at 50°C and pH 10.5 are 1.6 mM and 0.13 mM, respectively. The nucleotide sequence of this meso-DAPDH gene encodes a 326-amino acid peptide. When the gene was cloned and overexpressed in Escherichia coli Rosetta (DE3), the specific activity in the crude extract of the recombinant cells was about 18.0-fold higher than in the extract from U. thermosphaericus strain A1. This made more rapid and simpler purification of the enzyme possible.

DOI： 10.1186/2191-0855-1-43

Language：English   Publishing type：Research paper (international conference proceedings)  

Language：English   Publishing type：Research paper (international conference proceedings)  

Language：English   Publishing type：Research paper (scientific journal)  

We report that the lees in salmon fish sauce consist of Tyr and Phe. The concentration of free l-Tyr (2.0mM) was almost same as the saturated concentration (2.4mM) in water at 20°C. This result shows that lees are formed by Tyr precipitation due to its saturation in the sauce.

DOI： org/10.1016/j.jbiosc.2011.05.009

Language：English   Publishing type：Research paper (scientific journal)  

Methods with which to simply and rapidly assay L-aspartate (L-Asp) and D-aspartate (D-Asp) would be highly useful for physiological research and for nutritional and clinical analyses. Levels of L- and D-Asp in food and cell extracts are currently determined using high-performance liquid chromatography. However, this method is time-consuming and expensive. Here we describe a simple and specific method for using an L-aspartate dehydrogenase (L-AspDH) system to colorimetrically assay L-Asp and a system of three hyperthermophilic enzymes--aspartate racemase (AspR), L-AspDH, and L-aspartate oxidase (L-AO)--to assay D-Asp. In the former, the reaction rate of nicotinamide adenine dinucleotide (NAD(+))-dependent L-AspDH was measured based on increases in the absorbance at 438 nm, reflecting formation of formazan from water-soluble tetrazolium-1 (WST-1), using 1-methoxy-5-methylphenazinum methyl sulfate (mPMS) as a redox mediator. In the latter, D-Asp was measured after first removing L-Asp in the sample solution with L-AO. The remaining D-Asp was then changed to L-Asp using racemase, and the newly formed L-Asp was assayed calorimetrically using NAD(+)-dependent aspartate dehydrogenase as described above. This method enables simple and rapid spectrophotometric determination of 1 to 100 μM L- and D-Asp in the assay systems. In addition, methods were applicable to the L- and D-Asp determinations in some living cells and foods.

Language：English   Publishing type：Research paper (scientific journal)  

Language：English   Publishing type：Research paper (scientific journal)  

Language：English   Publishing type：Research paper (scientific journal)  

The activity of a dye-linked L: -proline dehydrogenase (dye-L: -proDH) was found in the crude extract of an aerobic hyperthermophilic archaeon, Pyrobaculum calidifontis JCM 11548, and was purified 163-fold through four sequential chromatography steps. The enzyme has a molecular mass of about 108 kDa and is a homodimer with a subunit molecular mass of about 46 kDa. The enzyme retained more than 90% of its activity after incubation at 100 °C for 120 min (pH 7.5) or after incubation at pHs 4.5-9.0 for 30 min at 50 °C. The enzyme catalyzed L: -proline dehydrogenation to Δ(1)-pyroline-5-carboxylate using 2,6-dichloroindophenol (DCIP) as the electron acceptor and the Michaelis constants for L: -proline and DCIP were 1.67 and 0.026 mM, respectively. The prosthetic group on the enzyme was identified as flavin adenine dinucleotide by high-performance liquid chromatography. The subunit N-terminal amino acid sequence was MYDYVVVGAG. Using that sequence and previously reported genome information, the gene encoding the enzyme (Pcal_1655) was identified. The gene was then cloned and expressed in Escherichia coli and found to encode a polypeptide of 415 amino acids with a calculated molecular weight of 46,259. The dye-L: -proDH gene cluster in P. calidifontis inherently differs from those in the other hyperthermophiles reported so far.

Language：English   Publishing type：Research paper (scientific journal)  

Thermus thermophilus cells formed siliceous deposits in the presence of supersaturated silicic acid (600 ppm SiO2). The supersaturated silicic acid promoted interaction between cells and the inside walls of glass culture bottles, leading to the development of cell aggregates or biofilms. Electron probe　micro analysis (EPMA) showed that within the aggregates most of the cell surfaces were covered with silica. Under these conditions, there was remarkable production of silica-induced protein (Sip), a solute-binding component of the Fe3+-binding ABC transporter. Furthermore, supersaturated silica enhanced resistance to the peptide antibiotics bacitracin, colistin and polymyxin B, which all act upon the cell envelope. By contrast, supersaturated silica did not induce resistance to ampicillin, chloramphenicol, kanamycin and tetracycline, which inhibit peptide synthesis. Although strong expression of Sip was detected in liquid cultures of T. thermophilus in the presence of supersaturated silica and colistin, upregulated transcription of putative efflux pump and multidrug resistance ABC transporter genes were not detected by quantitative real-time PCR analysis. These findings suggest Sip promotes silica deposition on the surfaces of cells, after which the silicified outer membrane may serve as a “suit-of-armor,” conferring resistance to peptide antibiotics.

Language：English   Publishing type：Research paper (scientific journal)  

The adhesion of Escherichia coli onto quartz, hematite and corundum was experimentally investigated. A strain of E. coli was used that had the genes for expressing protein for silica precipitation. The maximum cell adhesion was observed at pH <4.3 for quartz and at pH 4.5–8.5 for corundum. For hematite, cell adhesion remained low at all pH values. The microbe–mineral adhesion was assessed by the extended DLVO theory approach. The essential parameters for calculation of microbe–mineral interaction energy (Hamaker constants and acid–base components) were experimentally determined. The extended DLVO approach could be used to explain the results of the adhesion experiments. The effect of E. coli on the floatability of three oxide minerals was determined and the results showed that E. coli can act as a selective collector for quartz at acidic pH values, with 90% of the quartz floated at 1.5 × 109 cells/ml. However, only 9% hematite and 30% corundum could be floated under similar conditions. By using E. coli and no reagents, it was possible to separate quartz from a hematite–quartz mixture with Newton's efficiency of 0.70. Removal of quartz from the corundum mixture was achieved by E. coli with Newton's efficiency of 0.62.

DOI： 10.1016/j.colsurfb.2009.07.009

Language：English   Publishing type：Research paper (scientific journal)  

The effects of silicic acid on the growth of Thermus thermophilus TMY, an extreme thermophile isolated from a siliceous deposit formed from geothermal water at a geothermal power plant in Japan, were examined at 75 degrees C. At concentrations higher than the solubility of amorphous silica (400 to 700 ppm SiO(2)), a silica-induced protein (Sip) was isolated from the cell envelope fraction of log-phase TMY cells grown in the presence of supersaturated silicic acid. Two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the molecular mass and pI of Sip to be about 35 kDa and 9.5, respectively. Induction of Sip expression occurred within 1 h after the addition of a supersaturating concentration of silicic acid to TM broth. Expression of Sip-like proteins was also observed in other thermophiles, including T. thermophilus HB8 and Thermus aquaticus YT-1. The amino acid sequence of Sip was similar to that of the predicted solute-binding protein of the Fe(3+) ABC transporter in T. thermophilus HB8 (locus tag, TTHA1628; GenBank accession no. NC_006461; GeneID, 3169376). The sip gene (987-bp) product showed 87% identity with the TTHA1628 product and the presumed Fe(3+)-binding protein of T. thermophilus HB27 (locus tag TTC1264; GenBank accession no. NC_005835; GeneID, 2774619). Within the genome, sip is situated as a component of the Fbp-type ABC transporter operon, which contains a palindromic structure immediately downstream of sip. This structure is conserved in other T. thermophilus genomes and may function as a terminator that causes definitive Sip expression in response to silica stress.

Other Link： http://aem.asm.org/cgi/content/abstract/75/8/2406

Language：English   Publishing type：Research paper (scientific journal)  

Other Link： http://ijs.sgmjournals.org/cgi/content/full/59/5/1007

Language：English   Publishing type：Research paper (scientific journal)  

Other Link： http://aem.asm.org/cgi/content/abstract/75/6/1758

Language：English   Publishing type：Research paper (scientific journal)  

Zeta potential measurements of silica-induced protein (SIP) Escherichia coli and quartz showed that the former are positively charged under acidic condition and negatively charged under neutral and alkaline conditions, with an isoelectric point (IEP) at pH 4.5, while the quartz was always negatively charged. Adsorption experiments with bacteria cells on quartz were conducted under different conditions. The results show that at pH values lower than the IEP of the cells, more cells were adsorbed due to electrostatic forces. However, at pH > 4.5, the amount of adsorbed cells decreased as a result of electrostatic repulsion forces. Zeta potentials of quartz showed that at pH 2.5 a significant change in the surface chemistry of quartz occurred after bacterial treatment. The degree of this change was related to the initial SIP E. coli concentration; at 5 × 107 cells/ml the average zeta potential of biotreated quartz shifted from –30 mV to 0 mV and at higher concentrations the zeta potential shifted to the positive direction and reached a similar value to that of the bacterial cells. SIP E. coli showed hydrophobic properties at pH lower than the IEP, with approximately 60% of the cells moving to the organic phase from aqueous phase. Bioflotation of quartz using SIP E. coli alone at pH 2.5 gave approximately 60% recovery because at this pH more bacteria adsorb onto the quartz surface and the bacterial surface is hydrophobic. In anionic flotation of quartz using sodium dodecyl sulfate, SIP E. coli cells act as a surface modifier, with an increase in flotation recovery from 28% to 85%. This is because the bacterial cells confer hydrophobic properties to the quartz and the biotreated quartz is positively charged, so a large amount of the collector was adsorbed and the recovery increased.

DOI： 10.1016/j.mineng.2007.10.019

Language：English   Publishing type：Research paper (scientific journal)  

Language：English   Publishing type：Research paper (scientific journal)  

Aims: To identify an extreme thermophile, strain TMY, isolated from silica scale from the geothermal electric power plant and to examine microdiversity of Thermus thermophilus strains.

Materials and Results: The isolated strain TMY was identified by morphological, biochemical and physiological tests. Phylogenetic comparison of the strain and other Thermus strains with 16S rDNA analysis, RAPD and ERIC-PCR fingerprinting were performed. Strain TMY was closely related to strain which was isolated from a hot spring in New Zealand and shown to belong to the Japanese Thermus cluster. However, there were considerable genetic differences between strain TMY and other Thermus species using DNA fingerprinting.

Conclusions: Based on morphological, physiological and genetic properties, strain TMY could be a strain of T. thermophilus. The distinct properties of strain TMY suggest that microdiversity of T. thermophilus strains should be considered.

Significance and Impact of the Study: The results of this study have demonstrated genetic diversity within T. thermophilus strains, which were previously masked by an almost identical 16S rDNA sequence. RAPD and ERIC-PCR could be potential methods for distinguishing between Thermus strains.

Other Link： http://www3.interscience.wiley.com/journal/119417709/abstract

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Repository Public URL： http://hdl.handle.net/2324/4511

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DOI： 10.1263/jbb.93.434

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DOI： 10.1016/S0923-2508(01)01252-9

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DOI： 10.2323/jgam.47.143

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DOI： 10.1271/bbb.65.247

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DOI： 10.1111/j.1574-6968.2000.tb09275.x

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DOI： 10.1271/bbb.64.751

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43(1・2), 217-225

Repository Public URL： http://hdl.handle.net/2324/24267

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DOI： 10.1111/j.1574-6968.1998.tb13305.x

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DOI： 10.1016/S0922-338X(98)80029-9

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DOI： 10.1271/bbb.62.1597

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DOI： 10.1271/bbb.62.1271

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Repository Public URL： http://hdl.handle.net/2324/24235

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DOI： 10.1016/S0167-4781(97)00089-4

Language：English   Publishing type：Research paper (scientific journal)  

Spontaneous phage-resistant mutants were isolated from Lactobacillus paracasei LPC by agar plate (AP) and secondary-culture (SC) methods. They were characterized by cell and colony morphologies, carbohydrate fermentation patterns, phage resistance stability, efficiency of plaquing (EOP), acidifying and milk acidification kinetics. Only 98 out of 175 isolates (56%) proved to be true phage-resistant mutants and the SC method was more efficient than the AP method. Although the phage resistance stability varied among the mutants isolated, the EOP values were mostly very high (<10
⁻¹¹
). Three phage-resistant strains were selected based on their extreme resistance capacity to the phage ΦT25 (EOP<10
⁻¹⁰
) and their nonlysogenic property. Acidifying activity did not differ between phage-sensitive strains and their three respective phage-resistant derivatives. Most of the mutants were completely or partially unable to adsorb phage particles. Restriction-modification type systems were not detected in all phage-resistant derivatives. All three selected mutants were identical to the corresponding parent strain of L. paracasei LPC in the cell and colony morphologies. The comparison of random amplified polymorphic DNA profiles obtained with four arbitrary primers also revealed the highest similarity coefficient (87%) among the parent strain and the three mutants, indicating that each mutant has been derived from this parent strain. A good performance during milk fermentation and the subsequent refrigerated storage were obtained when these mutants were employed. These phage-resistant derivatives could be used as improved strains or for strain rotation programs when commercial strains become sensitive to the phages present in industrial environments.

DOI： 10.1016/j.foodcont.2018.12.037

Language：English   Publishing type：Research paper (scientific journal)  

Indigo is an insoluble blue dye historically used for dyeing textiles. A traditional approach for indigo dyeing involves microbial reduction of polygonum indigo to solubilize it under alkaline conditions; however, the mechanism by which microorganisms reduce indigo remains poorly understood. Here, we aimed to identify an enzyme that catalyzes indigo reduction; for this purpose, from alkaline liquor that performed microbial reduction of polygonum indigo, we isolated indigo carmine-reducing microorganisms. All isolates were facultative anaerobic and alkali-tolerant Bacillus spp. An isolate termed AO1 was found to be an alkaliphile that preferentially grows at pH 9.0–11.0 and at 30–35 °C. We focused on flavin-dependent azoreductase as a possible enzyme for indigo carmine reduction and identified its gene (azoA) in Bacillus sp. AO1 using homology-based strategies. azoA was monocistronic but clustered with ABC transporter genes. Primary sequence identities were < 50% between the azoA product (AzoA) and previously characterized flavin-dependent azoreductases. AzoA was heterologously produced as a flavoprotein tolerant to alkaline and organic solvents. The enzyme efficiently reduced indigo carmine in an NADH-dependent manner and showed strict specificity for electron acceptors. Notably, AzoA oxidized NADH in the presence, but not the absence, of indigo. The reaction rate was enhanced by adding organic solvents to solubilize indigo. Absorption spectrum analysis showed that indigo absorption decreased during the reaction. These observations suggest that AzoA can reduce indigo in vitro and potentially in Bacillus sp. AO1. This is the first study that identified an indigo reductase, providing a new insight into a traditional approach for indigo dyeing.

DOI： 10.1007/s00253-018-9284-y

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DOI： 10.1016/j.foodcont.2016.10.052

Language：English   Publishing type：Research paper (scientific journal)  

Mushrooms have garnered immense popularity for their nutritional as well as medicinal values. The therapeutic potential of mushrooms in Nepal, a country well known for its biodiversity and natural medicinal resources, remains largely unstudied. Therefore, this study attempts to unveil the antioxidative properties of Nepalese wild mushrooms. Sixty-two wild mushroom samples were collected from several forests in different parts of Nepal. Ethanol and water extracts of the dried samples were tested for their antioxidative activities using total phenolic content (TPC), oxygen radical absorbance capacity (ORAC) assay, 2,2-diphenyl-1-picrylhydrazyl (DPPH), 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), and reducing power (RP) assays. Ethanol extracts of samples belonging to the order Hymenochaetales showed significantly high activity in all the assays. Inonotus clemensiae had an exceptionally high TPC of 643.2 mg gallic acid equivalent (GAE)/g extract and also exhibited the lowest EC₅₀ values in DPPH (0.081 mg/mL), ABTS (0.409 mg/mL), and EC_0.5 value in reducing power (RP; 0.031 mg/mL) assays. High-performance liquid chromatography (HPLC) analysis of the top ten samples with the highest TPC was done to identify the phenolic compounds in the extracts, followed by liquid chromatography–mass spectrometry (LC–MS) analysis for some unknown compounds. These findings highlight the very strong antioxidative activity of Nepalese mushrooms, and paves the way for further research to explore their economic potential.

DOI： 10.1007/s11418-016-1013-1

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DOI： 10.1128/AEM.02577-14

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DOI： 10.1111/j.1574-6941.1997.tb00421.x

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DOI： 10.1111/j.1574-6968.1996.tb08156.x

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DOI： 10.1111/j.1365-2672.1995.tb03132.x

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Repository Public URL： http://hdl.handle.net/2324/24051

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Language：Japanese   Book type：Scholarly book

The World of Microorganisms

Responsible for pages：形質導入（ファージ取扱い技術）, p.52-55   Language：Japanese   Book type：Scholarly book

Responsible for pages：「微生物の構造」、p.89-94   Language：Japanese   Book type：Scholarly book

Responsible for pages：「遺伝子ターゲッティング」p218-221   Language：Japanese   Book type：Scholarly book

Responsible for pages：p1-112   Language：Japanese   Book type：Scholarly book

Responsible for pages：p1-129   Language：Japanese   Book type：Scholarly book

Responsible for pages：「微生物の遺伝子ターゲッティング」p. 1-38   Language：Japanese   Book type：Scholarly book

Event date： 2023.8

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：弘前大学50 周年記念会館   Country：Japan  

Event date： 2023.8

Language：English   Presentation type：Oral presentation (general)  

Venue：弘前大学50 周年記念会館   Country：Japan  

Event date： 2023.7 - 2024.7

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2023.7 - 2024.7

Language：English   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2023.7 - 2024.7

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2023.3

Language：English   Presentation type：Oral presentation (general)  

Venue：Kyungsung University   Country：Korea, Republic of  

Event date： 2022.11

Language：English   Presentation type：Oral presentation (general)  

Venue：オンライン   Country：Japan  

Event date： 2022.11

Language：English   Presentation type：Oral presentation (general)  

Venue：オンライン   Country：Japan  

Event date： 2022.10

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：オンライン   Country：Japan  

Event date： 2022.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：オンライン   Country：Japan  

Event date： 2022.3

Language：Japanese   Presentation type：Symposium, workshop panel (public)  

Venue：オンライン   Country：Japan  

Event date： 2021.12

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：別府大学 食物栄養科学部   Country：Japan  

Event date： 2021.12

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：別府大学 食物栄養科学部   Country：Japan  

Event date： 2021.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：オンライン   Country：Japan  

Event date： 2021.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：オンライン   Country：Japan  

Event date： 2021.7

Language：English   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2021.7

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2020.12 - 2019.12

Language：English   Presentation type：Oral presentation (general)  

Venue：オンライン   Country：Japan  

Event date： 2019.12

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：長崎大学 水産学部   Country：Japan  

Event date： 2019.11

Language：English   Presentation type：Oral presentation (general)  

Venue：福岡市科学館   Country：Japan  

Event date： 2019.11

Language：English   Presentation type：Oral presentation (general)  

Venue：福岡市科学館   Country：Japan  

Event date： 2019.11

Language：English   Presentation type：Oral presentation (general)  

Venue：琉球大学人文社会学部   Country：Japan  

Event date： 2019.7

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2019.7

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2019.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：東京農業大学   Country：Japan  

Event date： 2019.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：東京農業大学   Country：Japan  

Event date： 2019.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：オンライン   Country：Japan  

Event date： 2019.3

Language：English   Presentation type：Oral presentation (general)  

Venue：オンライン   Country：Japan  

Event date： 2018.11

Language：English   Presentation type：Oral presentation (general)  

Venue：福岡市科学館   Country：Japan  

Event date： 2018.11

Language：English   Presentation type：Oral presentation (general)  

Venue：福岡市科学館   Country：Japan  

Event date： 2018.6

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2018.6

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2018.6

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2018.3 - 2016.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：名城大学 天白キャンパス   Country：Japan  

Event date： 2018.3 - 2016.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：名城大学 天白キャンパス   Country：Japan  

Event date： 2018.3 - 2016.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：名城大学 天白キャンパス   Country：Japan  

Event date： 2018.3 - 2016.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：名城大学 天白キャンパス   Country：Japan  

Event date： 2018.3 - 2016.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：名城大学 天白キャンパス   Country：Japan  

Event date： 2018.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：京都大学 桂キャンパス 船井哲良記念講堂   Country：Japan  

Event date： 2017.12 - 2016.12

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：琉球大学農学部   Country：Japan  

Event date： 2017.12 - 2016.12

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：神戸国際展示場   Country：Japan  

Event date： 2017.9

Language：English   Presentation type：Oral presentation (general)  

Venue：大阪府立大学   Country：Japan  

Event date： 2017.7

Language：Japanese   Presentation type：Symposium, workshop panel (public)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2016.12

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：九州工業大学 情報工学部   Country：Japan  

Event date： 2016.11 - 2016.12

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：パシフィコ横浜   Country：Japan  

Event date： 2016.11

Language：English   Presentation type：Oral presentation (general)  

Venue：Hotel Interciti   Country：Korea, Republic of  

Event date： 2016.11

Language：English   Presentation type：Oral presentation (general)  

Venue：Hotel Interciti   Country：Korea, Republic of  

Event date： 2016.10

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：JAMSTEC 横浜研究所三好記念講堂   Country：Japan  

Event date： 2016.10

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：JAMSTEC 横浜研究所三好記念講堂   Country：Japan  

Event date： 2016.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：長崎大学   Country：Japan  

Event date： 2016.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：長崎大学   Country：Japan  

Event date： 2016.7

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2016.7

Language：English   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2016.6 - 2015.6

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2016.6 - 2015.6

Language：English   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2016.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：札幌コンベンションセンター   Country：Japan  

Event date： 2016.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：札幌コンベンションセンター   Country：Japan  

Event date： 2016.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：札幌コンベンションセンター   Country：Japan  

Event date： 2016.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：札幌コンベンションセンター   Country：Japan  

Event date： 2016.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：札幌コンベンションセンター   Country：Japan  

Event date： 2016.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：札幌コンベンションセンター   Country：Japan  

Event date： 2016.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：札幌コンベンションセンター   Country：Japan  

Event date： 2016.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：東京工業大学　大岡山キャンパス   Country：Japan  

Event date： 2015.12

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：ANAホリデイ・イン リゾート 宮崎   Country：Japan  

Event date： 2015.12

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：ANAホリデイ・イン リゾート 宮崎   Country：Japan  

Event date： 2015.12

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：宮崎大学 農学部   Country：Japan  

Event date： 2015.12

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：宮崎大学 農学部   Country：Japan  

Event date： 2015.10

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：城山観光ホテル   Country：Japan  

Event date： 2015.10

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：城山観光ホテル   Country：Japan  

Event date： 2015.10

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：城山観光ホテル   Country：Japan  

Event date： 2015.10

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：城山観光ホテル   Country：Japan  

Event date： 2014.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：佐賀大学   Country：Japan  

Event date： 2014.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：佐賀大学   Country：Japan  

Event date： 2014.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：三重大学生物資源学部   Country：Japan  

Event date： 2014.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：三重大学生物資源学部   Country：Japan  

Event date： 2014.8

Language：English   Presentation type：Oral presentation (general)  

Venue：University of Wisconsin, Madison   Country：United States  

This research attempts to clone a novel endolysin from phage φOH2 and to perform characterization and functional analysis of the enzyme. φOH2 endolysin is found to be an extremely thermostable enzyme carrying PGRP domain, capable of degrading cell wall of bacteria other than phage’s host and withstand treatment in various pH buffers. Further work on this particular enzyme could help in understanding heat resistant mechanism of thermostable endolysin and developing a new antibacterial agent that could target antibiotic-resistant bacteria.

Event date： 2014.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：明治大学　生田キャンパス   Country：Japan  

Event date： 2014.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：岡山大学　津島キャンパス   Country：Japan  

Event date： 2014.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：岡山大学　津島キャンパス   Country：Japan  

Event date： 2014.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：岡山大学　津島キャンパス   Country：Japan  

Event date： 2014.3

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：岡山大学　津島キャンパス   Country：Japan  

Event date： 2013.12

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：佐賀大学   Country：Japan  

Event date： 2013.11

Language：English   Presentation type：Oral presentation (general)  

Venue：サンホテルフェニックス   Country：Japan  

Event date： 2013.11

Language：Japanese   Presentation type：Symposium, workshop panel (public)  

Venue：高知大学   Country：Japan  

Event date： 2013.10

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：常翔学園大阪センター   Country：Japan  

Event date： 2013.10

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：常翔学園大阪センター   Country：Japan  

Event date： 2013.10

Language：English   Presentation type：Oral presentation (general)  

Venue：Faculty of Medicine、 Complutense University in Madrid   Country：Spain  

Event date： 2013.9

Language：English   Presentation type：Oral presentation (general)  

Venue：University of Regensburg   Country：Germany  

Event date： 2013.7 - 2014.6

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2013.7 - 2014.6

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2013.7

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2012.12

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：別府大学　メディアホール　39号館   Country：Japan  

Event date： 2012.12

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：別府大学　メディアホール　39号館   Country：Japan  

Event date： 2012.12

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：別府大学   Country：Japan  

Event date： 2012.10

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：神戸国際会議場   Country：Japan  

Event date： 2012.10

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：神戸国際会議場   Country：Japan  

Event date： 2012.9

Presentation type：Symposium, workshop panel (public)  

Venue：富山国際会議場   Country：Japan  

Event date： 2012.3

Presentation type：Oral presentation (general)  

Venue：京都女子大学   Country：Japan  

Event date： 2012.3

Presentation type：Oral presentation (general)  

Venue：京都女子大学   Country：Japan  

Event date： 2012.3

Presentation type：Oral presentation (general)  

Venue：京都女子大学   Country：Japan  

Event date： 2012.3

Presentation type：Oral presentation (general)  

Venue：立教大学   Country：Japan  

本研究では、臨海域の熱水に特徴的な微生物を解析することを目的として、様々な臨海域熱水中の微生物を収集し、16SrDNA領域のシーケンス解析を行うことによって、各熱水における微生物叢の特徴付けを行ってきた。
サンプル収集及びDNA解析は、以下のように行った。鹿児島県山川地熱発電所各生産井より熱水を採取し、0.1%のTryptone及びYeast extract を添加して、70℃及び80℃で往復振とう培養（160rpm)した。これと同時に、環境DNAの採取・保存が可能なFTA card (Whatman社製)に採取熱水を塗抹した。また、山川発電所内熱水ピット堆積物、鹿児島県指宿市内の玉手箱温泉源泉、湯権現付近の源泉からのサンプルに対しても同様の操作を行った。これらの集積培養にて増殖が見られた培養液からゲノムDNAを抽出し、16SrRNA増幅用プライマー（27F、1492R）を用いて16SrDNA領域をPCRによって増幅した。得られたPCR産物を精製しパイロシークエンス法により塩基配列を決定した。
収集した配列情報を用いて、RDPのclassifierによる微生物分類やBlast相同性検索による分類・同定を行った。各熱水中における微生物叢の相違点や特徴について報告する。

Event date： 2012.3

Presentation type：Oral presentation (general)  

Venue：立教大学   Country：Japan  

Event date： 2011.12

Presentation type：Oral presentation (general)  

Venue：九州大学工学部 総合学習プラザ   Country：Japan  

Event date： 2011.9

Presentation type：Oral presentation (general)  

Venue：宮崎大学   Country：Japan  

Event date： 2011.7

Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2011.7

Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2011.7

Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Event date： 2011.6

Presentation type：Symposium, workshop panel (public)  

Venue：Homerton College, Cambridge   Country：United Kingdom  

Event date： 2011.6

Presentation type：Symposium, workshop panel (public)  

Venue：Homerton College, Cambridge   Country：United Kingdom  

Event date： 2011.3

Presentation type：Oral presentation (general)  

Venue：東北大学   Country：Japan  

自然界の高温環境から収集した多数の土壌試料を用いて、meso-ジアミノピメリン酸脱水素酵素（DAPDH）を生産する好熱菌を広範にスクリーニングした結果、DAPDHを生産する好熱菌を初めて見出した。この好熱菌は16S rRNAの塩基配列の相同性解析からU. thermosphaericusと同定した。ペプトンなどを主成分とする栄養培地で好気的に簡便に培養できる方法を確立した。培養して得た菌体を超音波破砕後、遠心分離し、上清を粗酵素液とし、陰イオン交換クロマトグラフィー(DEAE TOYOPEARL)、及び調製用電気泳動法（Native-PAGE）を用いてDAPDHを電気泳動的に均一に精製することに成功した。
　SDS-PAGEとゲルろ過クロマトグラフィーにより分子質量を決定し、本酵素が40 kDaのサブユニットから成る二量体構造をとることを明らかにした。基質特異性、至適pH、熱安定性などの酵素化学的な基本的性質を解析した結果、本酵素は補酵素としてNADPを利用し、電子供与体としてはmeso-ジアミノピメリン酸に特異的であった。またpH 10.5において最大活性が認められた。65ºC(30分間処理)の温度まで、変性失活が認められなかった。本酵素は、既知の常温菌由来のDAPDHと比較して、類似の分子質量、基質特異性、至適pHを示す熱安定性が格段に高い耐熱性DAPDHを本研究により発見できた。

Event date： 2011.3

Presentation type：Oral presentation (general)  

Venue：東北大学   Country：Japan  

[目的]　近年、エネルギー生産や環境保全に対する意識が世界的規模で高まる中で、未利用生物資源を燃料源とし、酵素や微生物を電極素子として用いるバイオ燃料電池は、少ない環境負荷でエネルギーを産生できる利点を有する。これまでグルコースなどの糖類を燃料とする脱水素酵素電池の開発研究が行われてきた。しかし、出力が小さく、酵素の安定性が低いなどの問題がある。そこで本研究では、食品廃棄物中に存在する未利用タンパク質やアミノ酸を燃料源とする酵素電池の開発を目指し、安定性に優れた耐熱性アミノ酸脱水素酵素を用いるアミノ酸燃料電池の作製を進めた。
[方法と結果]　アミノ酸燃料電池として、まずL-プロリン酵素電池を作製した。アノード用素子として超好熱菌Pyrococcus horikoshii由来のL-プロリン脱水素酵素(α4β4構造)のβサブユニットを、カソードには白金を用い、DCIPをメディエータとする酵素電池を構築した。その結果、50℃で起電力0.45V、最大出力35μW/cm2のL-プロリン酵素電池の開発に成功した。

Event date： 2010.9

Presentation type：Oral presentation (general)  

Venue：崇城大学   Country：Japan  

Event date： 2010.7

Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Other Link： http://www.agr.kyushu-u.ac.jp/jsbba-west/47godo.html

Event date： 2010.6

Presentation type：Oral presentation (general)  

Venue：Knoxville Convention Center, Knoxville, Tennessee   Country：United States  

Thermus thermophilus TMY, an extreme thermophile, was isolated from a siliceous deposit formed from geothermal water at a geothermal power plant. At concentrations higher than the solubility of amorphous silica (400 to 700 ppm SiO2, at 750), a silica-induced protein (Sip) was expressed in the cell envelope of log-phase cells grown in the presence of supersaturated silicic acid. Molecular weightand pI of Sip were about 35 kDa and 9.5, respectively. Induction of Sip expression occurred within 1 h after the addition of a supersaturating concentration of silicic acid to broth. Production of Sip and its upregulation were in excellent temporal agreement with the silica precipitation, which was observed at silicic acid concentrations greater than 400 ppm in the medium at 75°C.
The amino acid sequence of Sip was similar to that of the predicted solute-binding protein of the Fe3+ -ABC transporter in T. thermophilus HB8 and HB27 [2]. Within the genome, sip is situated as a component of the Fbp-type ABC transporter operon, which contains a palindromic structure immediately downstream of sip. This structure is conserved in other T. thermophilus genomes and may function as a terminator that causes definitive Sip expression in response to silica stress.
　　　　　The sip gene was cloned in pET32 and expressed in E. coli. Transformant grown in LB containing 600 ppm silica precipitated silica during their growth (Fig. 1). Purified and heat-treated Sip protein also precipitated silica effectively. Therefore Sip might exhibit their silica precipitation ability.

Other Link： http://goldschmidt2010.org/

Event date： 2010.6

Presentation type：Oral presentation (general)  

Venue：Knoxville Convention Center, Knoxville, Tennessee   Country：United States  

The genus Thermus are defined as aerobic, heterotrophic, non-motile, pigmented, non-spore-forming, and Gram- negative rods that can grow at temperatures over 70 °C. Previously, we isolated Thermus thermuohilus TMY from the geothermal power plant in Japan and reported that strain TMY induces the precipitation of supersaturated silicic acid during exponeatial growth phase.
Notably, supersaturated silicic acid markedly stimulated expression of one cell envelope protein, which is named as silica-induced protein (Sip). The amino acid sequence of Sip showed significant
similarity with the solute-binding protein of Fe3+ ABC transporters observed in other Thermus strains, however, little is known about the regulation of gene expression in response to supersaturated silicic acid. To determine the regulation of Sip expression, the transdriptional regulation mechanisms were investigated.
Althogh sip operon comprises sip (solute-binding protein), permiase and ATPase, only sip gene was strongly transcribed in the silica-stressed condition. This might result from the fact that the palindromic structure located immidiately downstream of sip could function as the terminator of sip. Primer extension analysis revealed that transcription initiation site of sip is
located at 34 bases upstream of start codon. -35 and -10 element of the sip promoter showed meaningful similarity to those of &A promoters commonly seen in T. thermophilus. Sip trnscription was enhanced by the addition of supersaturated silicic acid, however, sip was also transcribed in the iron-condition. Due to the negative charge of colloidal silica in silica-stressed condition, iron ions might be trapped by colloidal silica. Thermus cells might receive the signals of the existence of supersaturated silicic acid as the iron deficiency caused by colloidal silica. This mechanism of silica-responsible promoter could serve us more convenient and effective genetic tools for thermophile and must shed new light on bacterial biosilicification studies.

Other Link： http://goldschmidt2010.org/

Event date： 2009.10

Presentation type：Oral presentation (general)  

Venue：琉球大学   Country：Japan  

Event date： 2009.10

Presentation type：Oral presentation (general)  

Venue：琉球大学   Country：Japan  

Event date： 2009.10

Presentation type：Oral presentation (general)  

Venue：琉球大学   Country：Japan  

Event date： 2009.10

Presentation type：Oral presentation (general)  

Venue：琉球大学   Country：Japan  

Event date： 2009.9

Presentation type：Oral presentation (general)  

Venue：名古屋大学   Country：Japan  

Event date： 2009.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：広島国際会議場   Country：Japan  

Event date： 2009.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：広島県立大学   Country：Japan  

Event date： 2009.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：広島県立大学   Country：Japan  

Event date： 2009.3

Presentation type：Oral presentation (general)  

Venue：琉球大学   Country：Japan  

Event date： 2009.3

Presentation type：Oral presentation (general)  

Venue：琉球大学   Country：Japan  

Event date： 2008.11

Presentation type：Oral presentation (general)  

Venue：忠南大学校   Country：Korea, Republic of  

Event date： 2008.11

Presentation type：Oral presentation (general)  

Venue：忠南大学校   Country：Korea, Republic of  

Event date： 2008.9

Presentation type：Oral presentation (general)  

Venue：九州大学西新プラザ   Country：Japan  

Event date： 2008.8

Presentation type：Oral presentation (general)  

Venue：東北学院大学土樋キャンパス   Country：Japan  

Event date： 2007.12

Presentation type：Oral presentation (general)  

Venue：崇城大学   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：福岡市   Country：Japan  

Presentation type：Symposium, workshop panel (public)  

Venue：福岡市   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：福岡国際会議場   Country：Japan  

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：HOTELグランデはがくれ   Country：Japan  

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：宮日会館ホール   Country：Japan  

Event date： 2013.11

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：名古屋・ウインクあいち   Country：Japan  

Event date： 2012.12

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：別府大学   Country：Japan  

Event date： 2012.10

Language：Japanese   Presentation type：Symposium, workshop panel (public)  

Venue：神戸国際会議場   Country：Japan  

Event date： 2010.12

Presentation type：Oral presentation (general)  

Venue：琉球大学   Country：Japan  

Event date： 2010.10 - 2008.8

Presentation type：Oral presentation (general)  

Venue：宮崎シーガイア　 ワールドコンベンションセンターサミット   Country：Japan  

Event date： 2009.9

Presentation type：Oral presentation (general)  

Venue：名古屋大学   Country：Japan  

Event date： 2009.3

Presentation type：Oral presentation (general)  

Venue：琉球大学   Country：Japan  

Event date： 2009.3

Presentation type：Oral presentation (general)  

Venue：琉球大学   Country：Japan  

Event date： 2009.3

Presentation type：Oral presentation (general)  

Venue：琉球大学   Country：Japan  

Event date： 2008.9

Presentation type：Oral presentation (general)  

Venue：長崎大学文教キャンパス   Country：Japan  

Event date： 2008.8

Presentation type：Oral presentation (general)  

Venue：東北学院大学土樋キャンパス   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：岡山大学（岡山市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：岡山大学（岡山市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：九州大学（福岡市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：九州大学（福岡市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：東北学院大学（仙台市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：東北学院大学（仙台市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：東北学院大学（仙台市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：東北学院大学（仙台市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：東北学院大学（仙台市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：つくば国際会議場（つくば市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：北海道地区国立大学大滝セミナーハウス（北海道有珠郡大滝村）  

Presentation type：Oral presentation (general)  

Venue：崇城大学（熊本市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：崇城大学（熊本市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：崇城大学（熊本市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：崇城大学（熊本市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：大阪国際会議場（大阪市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：大阪国際会議場（大阪市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：日本大学（藤沢市）   Country：Japan  

Genetic analysis of ABC transporter gene in Streptomyces azureus

Presentation type：Oral presentation (general)  

Venue：日本大学（藤沢市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：日本大学（藤沢市）   Country：Japan  

Identification of plasmid affected its host growth in Lactobacillus plantarum NGRI0101

Presentation type：Oral presentation (general)  

Venue：熊本大学（熊本市）   Country：Japan  

Characterization of plasmid pLKS in Lactobacillus plantarum NGRI0101

Presentation type：Oral presentation (general)  

Venue：鹿児島大学（鹿児島市）   Country：Japan  

Temporal and Spatial Expression of DNA translocase Gene in Streptomyces azureus

Presentation type：Oral presentation (general)  

Venue：鹿児島大学（鹿児島市）   Country：Japan  

Site-specific integration of lysogenic phage SAt2 in Streptomyces azureus

Presentation type：Oral presentation (general)  

Venue：熊本大学（熊本市）   Country：Japan  

Analysis of ABC transporter gene in Streptomyces azureus

Presentation type：Oral presentation (general)  

Presentation type：Oral presentation (general)  

Venue：京都市   Country：Japan  

Presentation type：Oral presentation (invited, special)  

Venue：淡路夢舞台国際会議場   Country：Japan  

Study on Temporal and Spatial Expression of the Sporulation-inhibitory Gene of Conjugative Plasmid During Differentiation in Streptomyces.

Award lecture for Hamada Award of Japan Society for Actinomycetes in 2004.

Presentation type：Oral presentation (general)  

Venue：福岡市   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：福岡市   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：福岡市   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：株式会社ヤクルト本社、伊東研修センター   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：ウイングウイング高岡   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：つくば 国際会議場   Country：Japan  

Presentation type：Symposium, workshop panel (public)  

Venue：京都女子大学   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：ＫＫＲ甲府ニュー芙蓉   Country：Japan  

Other Link： http://www.bio.eng.osaka-u.ac.jp/ps/LAB/main.html

Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Other Link： http://www.agr.kyushu-u.ac.jp/jsbba-west/43godo.html

Presentation type：Oral presentation (general)  

Venue：北九州国際会議場   Country：Japan  

Other Link： http://www.agr.kyushu-u.ac.jp/jsbba-west/43godo.html

Presentation type：Oral presentation (general)  

Venue：SPring-8   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：九州大学伊都キャンパス   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：九州大学伊都キャンパス   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：東京農業大学世田谷キャンパス   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：東京農業大学世田谷キャンパス   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：山口大学   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：山口大学   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：福岡市   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：福岡市   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：福岡市   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：名城大学天白キャンパス   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：名城大学天白キャンパス   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：崇城大学   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：崇城大学   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：崇城大学   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：崇城大学   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：崇城大学   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：マリンメッセ福岡   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：マリンメッセ福岡   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：マリンメッセ福岡   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：マリンメッセ福岡   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：岡山大学（岡山市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：マリンメッセ福岡（福岡市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：東京ビックサイト（東京都）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：東京ビックサイト（東京都）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：東京ビックサイト（東京都）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：福岡リーセントホテル（福岡市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：福岡リーセントホテル（福岡市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：福岡リーセントホテル（福岡市）   Country：Japan  

Presentation type：Symposium, workshop panel (public)  

Venue：北海道大学（札幌市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：北海道大学（札幌市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：琉球大学（沖縄県中頭郡西原町）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：琉球大学（沖縄県中頭郡西原町）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：琉球大学（沖縄県中頭郡西原町）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：山口大学（山口市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：山口大学（山口市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：立命館大学（京都市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：立命館大学（京都市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：立命館大学（京都市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：立命館大学（京都市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：立命館大学（京都市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：立命館大学（京都市）   Country：Japan  

Presentation type：Oral presentation (general)  

Venue：大阪大学（池田市）   Country：Japan  

Language：Japanese   Publishing type：Internal/External technical report, pre-print, etc.  

Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

Language：Japanese   Publishing type：Internal/External technical report, pre-print, etc.  

Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

Language：Japanese   Publishing type：Internal/External technical report, pre-print, etc.  

Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

Language：Japanese   Publishing type：Internal/External technical report, pre-print, etc.  

Language：Japanese   Publishing type：Internal/External technical report, pre-print, etc.  

Language：Japanese   Publishing type：Internal/External technical report, pre-print, etc.  

Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

Type：Peer review 

Number of peer-reviewed articles in foreign language journals：18

Number of peer-reviewed articles in Japanese journals：0

Proceedings of International Conference Number of peer-reviewed papers：0

Proceedings of domestic conference Number of peer-reviewed papers：0

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Number of participants：1,600

Type：Competition, symposium, etc. 

Number of participants：100

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Number of participants：80

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Number of participants：200

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Number of participants：50

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Type：Competition, symposium, etc. 

Number of participants：200